Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.
about
Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry.The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping.Methodologies for wiring redox proteins/enzymes to electrode surfaces.Conserved Histidine Adjacent to the Proximal Cluster Tunes the Anaerobic Reductive Activation of Escherichia coli Membrane-Bound [NiFe] Hydrogenase-1.An extracellular [NiFe] hydrogenase mediating iron corrosion is encoded in a genetically unstable genomic island in Methanococcus maripaludis
P2860
Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.
description
2017 nî lūn-bûn
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2017年の論文
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2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
2017年论文
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2017年论文
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name
Retuning the Catalytic Bias an ...... the Electron Entry/Exit Site.
@en
type
label
Retuning the Catalytic Bias an ...... the Electron Entry/Exit Site.
@en
prefLabel
Retuning the Catalytic Bias an ...... the Electron Entry/Exit Site.
@en
P2093
P2860
P50
P356
P6366
P1154
2-s2.0-85027160354
P1476
Retuning the Catalytic Bias an ...... the Electron Entry/Exit Site.
@en
P2093
Darrell Elton
David J Gavaghan
Hope Adamson
John J Wright
Julia Walton
Lindsey A Flanagan
Martin Robinson
P2860
P304
10677-10686
P356
10.1021/JACS.7B03611
P407
P577
2017-07-12T00:00:00Z
P6366
2735455959